Research workbench
Crystal structure of the complex of the CAF1M chaperone with the mini-fiber of two CAF1 subunits (CAF1:CAF1), carrying the THR7PHE mutation in the gd donor strand
Analyse Crystal structure of the complex of the CAF1M chaperone with the mini-fiber of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DSN
- Type
- protein
- Length
- 945 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein CAF1M; F1 capsule antigen
- UniProt
- P26926, P26948
- Pockets
- 9 · best druggability 0.62
Structure
x-ray diffraction · 6 distinct chains · 3% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein CAF1M | protein | 199 | 3% helix, 56% strand | P26926 |
| B | F1 capsule antigen | protein | 146 | 2% helix, 51% strand | P26948 |
| C | F1 capsule antigen | protein | 132 | 2% helix, 48% strand | P26948 |
| D | Chaperone protein CAF1M | protein | 190 | 3% helix, 58% strand | P26926 |
| E | F1 capsule antigen | protein | 149 | 2% helix, 54% strand | P26948 |
| F | F1 capsule antigen | protein | 129 | 2% helix, 49% strand | P26948 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.62 | 0.82 | 41 | empty |
| 2 | 304 | 0.54 | 0.75 | 46 | empty |
| 3 | 181 | 0.54 | 0.79 | 35 | empty |
| 4 | 200 | 0.51 | 0.77 | 22 | empty |
| 5 | 159 | 0.44 | 0.75 | 27 | empty |
Interfaces
8 interfaces between chains.
- D–E · 1754 Ų buried · 42 hydrogen bonds · protein-protein
- A–B · 1567 Ų buried · 39 hydrogen bonds · protein-protein
- B–C · 1211 Ų buried · 31 hydrogen bonds · protein-protein
- E–F · 1159 Ų buried · 29 hydrogen bonds · protein-protein
- B–D · 599 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3DSN · Crystal structure of the complex of the Caf1M chaperone with the mini-fiber of two Caf1… · the same entry in another collection · chain F against F, TM-score 1.00
- P26926 · AlphaFold monomer V2.0 prediction for chaperone protein CAF1M (P26926) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P26948 · AlphaFold monomer V2.0 prediction for F1 capsule antigen (P26948) · a predicted model of the same protein · chain F against A, TM-score 0.95
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P26926
- Every structure of UniProt P26948
- Elsewhere: RCSB PDB 3DSN · PDBe 3DSN · UniProt P26926 · UniProt P26948
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